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J Biol Chem, Vol. 274, Issue 29, 20215-20222, July 16, 1999
From the Department of Pharmacology and Cancer Biology, Duke
University Medical Center, Durham, North Carolina 27710 and
Phosphorylation of
Ca2+/calmodulin-dependent protein kinase
I (CaM KI) at Thr-177 by recombinant rat
Ca2+/calmodulin-dependent kinase kinase B (CaM KKB)
modulates the kinetics of synapsin-(4-13) peptide phosphorylation by
reducing the Km 44-fold and decreasing the
KCaM 4-fold. There is also a slight decrease in
Km for ATP and increase in enzyme
Vmax. A synthetic peptide substrate from the
yeast transcription factor, ADR1-(222-234)G233 is a 15-fold better
substrate for the Thr-177 dephospho-form of CaM KI than
synapsin-(4-13). The Thr-177 dephospho-enzyme has a
Km and Vmax for
ADR1-(222-234)G233 similar to the values with synapsin-(4-13) using
the Thr-177 phosphorylated enzyme. Likewise, with ADR1-(222-234)G233
as substrate, phosphorylation of Thr-177 or substitution of T177A had
very little effect on the kinetic values. Using chimeric peptides
between synapsin-(4-13) and ADR1-(222-234)G233 we found that
N-terminal basic residues at P
Peptide Specificity Determinants at P
7 and P6 Enhance the
Catalytic Efficiency of
Ca2+/Calmodulin-dependent Protein Kinase I
in the Absence of Activation Loop Phosphorylation
, and St. Vincent's Institute of Medical Research, Fitzroy,
Victoria 3065, Australia
7 and P6 positions were sufficient to
allow efficient phosphorylation by the Thr-177 dephospho-form of CaM
KI. Phosphorylation of Thr-177 expands the substrate specificity of CaM
KI and is not merely an "on-off" switch for kinase activity.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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